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Korasick, D. A., Končitíková, R., Kopečná, M., Hájková, E., Vigouroux, A., Moréra, S., Becker, D. F., Šebela, M., Tanner, J. J., and Kopečný, D. (2019) Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants. J Mol Biol. 431, 576-592
Korasick, D. A., Owuocha, L. F., Kandoth, P. K., Tanner, J. J., Mitchum, M. G., and Beamer, L. J. (2023) Structural and functional analysis of two SHMT8 variants associated with soybean cyst nematode resistance. FEBS J. 10.1111/febs.16971
Kono, A., Chou, T. - H., Radhakrishnan, A., Bolla, J. Reddy, Sankar, K., Shome, S., Su, C. - C., Jernigan, R. L., Robinson, C. V., Yu, E. W., and Spalding, M. H. (2020) Structure and Function of LCI1: A plasma membrane CO channel in the Chlamydomonas CO concentrating mechanism. Plant J. 10.1111/tpj.14745
Köksal, M., Hu, H., Coates, R. M., Peters, R. J., and Christianson, D. W. (2011) Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase. Nat Chem Biol. 7, 431-3
Koirala, D., Lewicka, A., Koldobskaya, Y., Huang, H., and Piccirilli, J. A. (2019) Synthetic Antibody Binding to a Preorganized RNA Domain of Hepatitis C Virus Internal Ribosome Entry Site Inhibits Translation. ACS Chem Biol. 10.1021/acschembio.9b00785
Kobe, M. J., Neau, D. B., Mitchell, C. E., Bartlett, S. G., and Newcomer, M. E. (2014) The structure of human 15-lipoxygenase-2 with a substrate mimic. J Biol Chem. 289, 8562-9
Knockenhauer, K. E., and Schwartz, T. U. (2015) Structural Characterization of Bardet-Biedl Syndrome 9 Protein (BBS9). J Biol Chem. 290, 19569-83
Knecht, K. M., Buzovetsky, O., Schneider, C., Thomas, D., Srikanth, V., Kaderali, L., Tofoleanu, F., Reiss, K., Ferreirós, N., Geisslinger, G., Batista, V. S., Ji, X., Cinatl, J., Keppler, O. T., and Xiong, Y. (2018) The structural basis for cancer drug interactions with the catalytic and allosteric sites of SAMHD1. Proc Natl Acad Sci U S A. 10.1073/pnas.1805593115
Knappenberger, A. John, Reiss, C. Wetheringt, and Strobel, S. A. (2018) Structures of two aptamers with differing ligand specificity reveal ruggedness in the functional landscape of RNA. Elife. 10.7554/eLife.36381
Klein, D. E., Choi, J. L., and Harrison, S. C. (2013) Structure of a dengue virus envelope protein late-stage fusion intermediate. J Virol. 87, 2287-93
Kiser, P. D., Farquhar, E. R., Shi, W., Sui, X., Chance, M. R., and Palczewski, K. (2012) Structure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis. Proc Natl Acad Sci U S A. 109, E2747-56
Kirouac, K. N., Basu, A. K., and Ling, H. (2013) Structural mechanism of replication stalling on a bulky amino-polycyclic aromatic hydrocarbon DNA adduct by a y family DNA polymerase. J Mol Biol. 425, 4167-76
Kirouac, K. N., and Ling, H. (2009) Structural basis of error-prone replication and stalling at a thymine base by human DNA polymerase iota. EMBO J. 28, 1644-54
King, N. P., Jacobitz, A. W., Sawaya, M. R., Goldschmidt, L., and Yeates, T. O. (2010) Structure and folding of a designed knotted protein. Proc Natl Acad Sci U S A. 107, 20732-7
Khare, B., Krishnan, V., Rajashankar, K. R., I-Hsiu, H., Xin, M., Ton-That, H., and Narayana, S. V. (2011) Structural differences between the Streptococcus agalactiae housekeeping and pilus-specific sortases: SrtA and SrtC1. PLoS One. 6, e22995
Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Keszei, A. F. A., Tang, X., McCormick, C., Zeqiraj, E., Rohde, J. R., Tyers, M., and Sicheri, F. (2014) Structure of an SspH1-PKN1 complex reveals the basis for host substrate recognition and mechanism of activation for a bacterial E3 ubiquitin ligase. Mol Cell Biol. 34, 362-73
Kenoth, R., Simanshu, D. K., Kamlekar, R. Kanth, Pike, H. M., Molotkovsky, J. G., Benson, L. M., H Bergen, R., Prendergast, F. G., Malinina, L., Venyaminov, S. Y., Patel, D. J., and Brown, R. E. (2010) Structural determination and tryptophan fluorescence of heterokaryon incompatibility C2 protein (HET-C2), a fungal glycolipid transfer protein (GLTP), provide novel insights into glycolipid specificity and membrane interaction by the GLTP fold. J Biol Chem. 285, 13066-78
Kavran, J. M., Gundllapalli, S., O'Donoghue, P., Englert, M., Söll, D., and Steitz, T. A. (2007) Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation. Proc Natl Acad Sci U S A. 104, 11268-73
Kavran, J. M., and Steitz, T. A. (2007) Structure of the base of the L7/L12 stalk of the Haloarcula marismortui large ribosomal subunit: analysis of L11 movements. J Mol Biol. 371, 1047-59
Kattke, M. D., Gosschalk, J. E., Martinez, O. E., Kumar, G., Gale, R. T., Cascio, D., Sawaya, M. R., Philips, M., Brown, E. D., and Clubb, R. T. (2019) Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria. PLoS Pathog. 15, e1007723
Kasznel, A. J., Zhang, Y., Hai, Y., and Chenoweth, D. M. (2017) Structural Basis for Aza-Glycine Stabilization of Collagen. J Am Chem Soc. 139, 9427-9430
Karasawa, A., and Kawate, T. (2016) Structural basis for subtype-specific inhibition of the P2X7 receptor. Elife. 10.7554/eLife.22153
Kapoor, N., Menon, S. T., Chauhan, R., Sachdev, P., and Sakmar, T. P. (2009) Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins. J Mol Biol. 393, 882-97
J
M Joyce, G., Bu, W., Chen, W. - H., Gillespie, R. A., Andrews, S. F., Wheatley, A. K., Tsybovsky, Y., Jensen, J. L., Stephens, T., Prabhakaran, M., Fisher, B. E., Narpala, S. R., Bagchi, M., McDermott, A. B., Nabel, G. J., Kwong, P. D., Mascola, J. R., Cohen, J. I., and Kanekiyo, M. (2025) Structural basis for complement receptor engagement and virus neutralization through Epstein-Barr virus gp350. Immunity. 58, 295-308.e5

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